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A fluorescent multi-domain protein reveals the unfolding mechanism of Hsp70

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A fluorescent multi-domain protein reveals the unfolding mechanism of Hsp70

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Statistical Analysis of Protein Sequences: A Coevolutionary Study of Molecular Chaperones

The Chaperone and Redox Properties of CnoX Chaperedoxins Are Tailored to the Proteostatic Needs of Bacterial Species

CnoX Is a Chaperedoxin: A Holdase that Protects Its Substrates from Irreversible Oxidation

Molecular chaperones inject energy from ATP hydrolysis into the non-equilibrium stabilisation of native proteins

Evolution of an intricate J-protein network driving protein disaggregation in eukaryotes

Thermodynamic bounds on the ultra- and infra-affinity of Hsp70 for its substrates

Experimental Milestones in the Discovery of Molecular Chaperones as Polypeptide Unfolding Enzymes

Cytoplasmic Ubiquitin-Specific Protease 19 (USP19) Modulates Aggregation of Polyglutamine-Expanded Ataxin-3 and Huntingtin through the HSP90 Chaperone

Automated longitudinal monitoring of in vivo protein aggregation in neurodegenerative disease C. elegans models

Large-Scale Conformational Transitions and Dimerization Are Encoded in the Amino-Acid Sequences of Hsp70 Chaperones